ID B0D777_LACBS Unreviewed; 519 AA.
AC B0D777;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EDR09350.1};
GN ORFNames=LACBIDRAFT_318835 {ECO:0000313|EMBL:EDR09350.1};
OS Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS (Laccaria laccata var. bicolor).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX NCBI_TaxID=486041 {ECO:0000313|Proteomes:UP000001194};
RN [1] {ECO:0000313|EMBL:EDR09350.1, ECO:0000313|Proteomes:UP000001194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 / ATCC MYA-4686 {ECO:0000313|Proteomes:UP000001194};
RX PubMed=18322534; DOI=10.1038/nature06556;
RA Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA Tuskan G., Grigoriev I.V.;
RT "The genome of Laccaria bicolor provides insights into mycorrhizal
RT symbiosis.";
RL Nature 452:88-92(2008).
CC -!- FUNCTION: Component of the FACT complex, a general chromatin factor
CC that acts to reorganize nucleosomes. The FACT complex is involved in
CC multiple processes that require DNA as a template such as mRNA
CC elongation, DNA replication and DNA repair. During transcription
CC elongation the FACT complex acts as a histone chaperone that both
CC destabilizes and restores nucleosomal structure. It facilitates the
CC passage of RNA polymerase II and transcription by promoting the
CC dissociation of one histone H2A-H2B dimer from the nucleosome, then
CC subsequently promotes the reestablishment of the nucleosome following
CC the passage of RNA polymerase II. {ECO:0000256|ARBA:ARBA00025370}.
CC -!- SIMILARITY: Belongs to the RTT106 family.
CC {ECO:0000256|ARBA:ARBA00006159}.
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DR EMBL; DS547099; EDR09350.1; -; Genomic_DNA.
DR RefSeq; XP_001879699.1; XM_001879664.1.
DR AlphaFoldDB; B0D777; -.
DR STRING; 486041.B0D777; -.
DR GeneID; 6075331; -.
DR KEGG; lbc:LACBIDRAFT_318835; -.
DR HOGENOM; CLU_020806_0_0_1; -.
DR InParanoid; B0D777; -.
DR OrthoDB; 1660359at2759; -.
DR Proteomes; UP000001194; Unassembled WGS sequence.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR013719; RTT106/SPT16-like_middle_dom.
DR PANTHER; PTHR45849; FACT COMPLEX SUBUNIT SSRP1; 1.
DR PANTHER; PTHR45849:SF3; HISTONE CHAPERONE RTT106; 1.
DR Pfam; PF08512; Rttp106-like_middle; 1.
DR SMART; SM01287; Rtt106; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001194}.
FT DOMAIN 274..379
FT /note="Histone chaperone RTT106/FACT complex subunit SPT16-
FT like middle"
FT /evidence="ECO:0000259|SMART:SM01287"
FT REGION 72..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..427
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..468
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..519
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 519 AA; 55859 MW; 84FE9AA87BC081C8 CRC64;
MASETEYLRA ILPSLPTGIA AKLRSLCATP ATESALENLV RFICGAQHSP EAPKEFHGEW
FEKQLTTRNL LKGMNWGSNS SENKRPRDDG AENQSESSKK PRISPAPVAT DGNPIYTLHS
ISTTSPIRKK VDITICENSI TFTNPSTRAS EGSVPRASIR RAFLVPTRGK SKPHWTVILL
SSDTPDRGKP ANPATPENPQ IIFGLDATST PPFTVTTYKS GSEPTPEVSP KGSTTLPFIH
AFFTHLGIAL FEPTVDVFKS ACVGIGNNVM AGNIPGVEAY RAAKSGSLWF TKEGILWGES
KPCEFWPVGS LISKSEGVRI IGGSGRTCSV VLTRKTESGS TGGDDEDMGE ETEFGMVDAR
EQEGIDRWVK KYRHLFGKTE GQSTDEAVDV ESKQPKKVQQ FGPVTINQLA AADDDDDDDD
DFAVDSDSES DGGSASPSSE DDEAGGSDGS DEEEGCEDGE GSDEEGEEEE LKPEHHPLLR
PGAMPKMSRA AMDMVVGMVE DDMMGGGSGE EDEEDELDD
//
